Thermodynamic analysis of the dissociation of the aldolase tetramer substituted at one or both of the subunit interfaces

Biological Chemistry

Volumn 384, Issue 10-11, 2003, Pages 1463-1471

  Tolan, Dean R ^a,b   Schuler, Benjamin ^b,c   Beernink, Peter T ^a,d   Jaenicke, Rainier ^b  

^a Boston University   (United States)

^b UNIVERSITY OF REGENSBURG   (Germany)

^c UNIVERSITY OF POTSDAM   (Germany)

^d LAWRENCE LIVERMORE NATIONAL LABORATORY   (United States)

Author keywords

Analytical ultracentrifugation; Dissociation constant; Protein stability; Quaternary structure; Site directed mutagenesis

Indexed keywords

FRUCTOSE BISPHOSPHATE ALDOLASE; MONOMER; TETRAMER;

ARTICLE; CATALYSIS; CONTROLLED STUDY; DISSOCIATION CONSTANT; ENERGY TRANSFER; ENZYME STRUCTURE; ENZYME SUBUNIT; MUTANT; NONHUMAN; PRIORITY JOURNAL; PROTEIN PROTEIN INTERACTION; SEDIMENTATION RATE; SUCROSE DENSITY GRADIENT CENTRIFUGATION; TEMPERATURE DEPENDENCE; THERMODYNAMICS; THERMOSTABILITY; ULTRACENTRIFUGE; WILD TYPE;

CENTRIFUGATION, DENSITY GRADIENT; ENZYME STABILITY; ESCHERICHIA COLI; FRUCTOSE-BISPHOSPHATE ALDOLASE; KINETICS; MUTAGENESIS, SITE-DIRECTED; PLASMIDS; PROTEIN STRUCTURE, QUATERNARY; PROTEIN SUBUNITS; TEMPERATURE; THERMODYNAMICS;

EID: 0344253687     PISSN: 14316730     EISSN: None     Source Type: Journal    
DOI: 10.1515/BC.2003.162     Document Type: Article

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